scholarly journals Ontogenesis of glomerular basement membrane: structural and functional properties.

1991 ◽  
Vol 113 (3) ◽  
pp. 689-700 ◽  
Author(s):  
M Desjardins ◽  
M Bendayan
Keyword(s):  
Basement Membrane ◽  
Functional Properties ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Protein A ◽  
Basement Membranes ◽  
Type Iv ◽  
Structural And Functional Properties ◽  
Entire Thickness ◽  
Filtration Properties

Protein A-gold immunocytochemistry was applied in combination with morphometrical approaches to reveal the alpha 1(IV), alpha 2(IV), and alpha 3(IV) chains of type IV collagen as well as entactin on renal basement membranes, particularly on the glomerular one, during maturation. The results have indicated that a heterogeneity between renal basement membranes appears during the maturation process. In the glomerulus at the capillary loop stage, both the epithelial and endothelial cell basement membranes were labeled for the alpha 1(IV) and alpha 2(IV) chains of type IV collagen and entactin. After fusion, both proteins were present on the entire thickness of the typical glomerular basement membrane. At later stages, the labeling for alpha 1(IV) and alpha 2(IV) chains of type IV collagen decreased and drifted towards the endothelial side, whereas the labeling for the alpha 3(IV) chain increased and remained centrally located. Entactin remained on the entire thickness of the basement membrane during maturation and in adult stage. The distribution of endogenous serum albumin in the glomerular wall was studied during maturation, as a reference for the functional properties of the glomerular basement membrane. This distribution, dispersed through the entire thickness of the basement membrane at early stages, shifted towards the endothelial side of the lamina densa with maturation, demonstrating a progressive acquisition of the permselectivity. These results demonstrate that modifications in the content and organization of the different constituents of basement membranes occur with maturation and are required for the establishment of the filtration properties of the glomerular basement membrane.

scholarly journals Developmental acquisition of basement membrane heterogeneity: type IV collagen in the avian lens capsule.

1983 ◽  
Vol 97 (3) ◽  
pp. 940-943 ◽  
Author(s):  
J M Fitch ◽  
R Mayne ◽  
T F Linsenmayer
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Lens Capsule ◽  
Basement Membranes ◽  
Developmentally Regulated ◽  
Membrane Heterogeneity ◽  
Domain Specific ◽  
Type Iv ◽  
Anterior Lens Capsule ◽  
Immunohistochemical Analyses

To investigate potential heterogeneity and developmental changes in basement membranes during embryogenesis, we performed immunohistochemical analyses on lens capsules in chicken embryos of different ages using domain-specific monoclonal antibodies against type IV collagen. We found that the capsule of the newly formed lens stained uniformly with antibodies against this component of basement membranes, but with increasing age and differentiation of the lens cells the anterior lens capsule remained brightly fluorescent while staining of the posterior capsule became relatively much less intense. This antero-posterior gradient of anti-type IV collagen antibody reactivity demonstrated that developmentally-regulated changes can occur within a single, continuous basement membrane.

IDENTIFICATION OF ??3, ??4, AND ??5 CHAINS OF TYPE IV COLLAGEN AS ALLOANTIGENS FOR ALPORT POSTTRANSPLANT ANTI-GLOMERULAR BASEMENT MEMBRANE ANTIBODIES

2000 ◽  
Vol 69 (4) ◽  
pp. 679-684 ◽  
Author(s):  
Raghu Kalluri ◽  
Adriana Torre ◽  
Charles F. Shield ◽  
Eric D. Zamborsky ◽  
Michelle C. Werner ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Type Iv

scholarly journals Glomerular Basement Membrane Selective Permeability in Short-term Streptozotocin-induced Diabetic Rats

2000 ◽  
Vol 1 (1) ◽  
pp. 19-30 ◽  
Author(s):  
Michele Doucet ◽  
Irene Londoño ◽  
Amparo Gómez-Pascual ◽  
Moise Bendayan
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Serum Proteins ◽  
Diabetic Rats ◽  
Glomerular Permeability ◽  
Structural Alterations ◽  
Early Stages ◽  
Type Iv ◽  
Basement Membrane Thickening

In diabetes, the glomerular basement membrane undergoes thickening and structural alterations with loss of glomerular permselectivity properties. However, the onset of the alterations at early phases of diabetes is unclear. Aiming to determine the functional and structural alterations of the glomerular wall in the early stages of diabetes, we have studied the distribution of endogenous circulating albumin and type IV collagen in the glomerular basement membrane, using the immunocytochemical approach. The streptozotocin-injected hyperglycemic rat was our animal model. Renal tissues were examined after 10 days, 2, 4 and 6 months of hyperglycemia. Upon immunogold labelings, changes in the glomerular permeability to endogenous albumin were found altered as early as upon ten days of hyperglycemia. In contrast, no structural modifications were detected at this time point. Indeed, glomerular basement membrane thickening and an altered type IV collagen labeling distribution were only observed after four months of hyperglycemia, suggesting that functional alterations take place early in diabetes prior to any structural modification. In order to evaluate the reversibility of the glomerular alterations, two-month-old diabetic animals were treated with insulin. These animals showed a significant restoring of their glomerular permselectivity. Our results suggest a link between glycemic levels and alteration of glomerular permeability in early stages of diabetes, probably through high levels of glycated serum proteins.

scholarly journals RETRACTED: Production and Characterization of Recombinant Rat Non-collagen Domain of α3 Chain of Type IV Collagen α3 (IV) NC1 Antigen

2016 ◽  
Vol 12 (24) ◽  
pp. 98
Author(s):  
Afsana Munni
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Kidney Diseases ◽  
Cell Epitope ◽  
Affinity Column ◽  
Igg Antibody ◽  
Amino Terminal ◽  
Type Iv ◽  
Collagenous Domain

Glomerulonephritis disease is characterized by inflammation of glomeruli or small blood vessels in the kidney which causes kidney diseases. Glomerulonephritis disease deposits the anti-GBM auto antibody in the glomerular basement membrane. The type IV collagen is the main component of glomerular basement membrane that has α3 chain of type (IV) collagen of non-collagenous domain which contains N-terminal 7S domain, a triple helical collagenous domain, and a C- terminal non-collagenous glomerular domain (NC1). The amino terminal of α3 (IV) NC1 that induces the experimental autoimmuno glomerulonephritis (EAG) in rat model has been identified. The recombinant rat α3 (IV)NC1 antigen has nine amino acid span that is consistent with antibody or T cell epitope which is induced in EAG. The research is carried out on the recombinant rat α3 (IV) NC1 production, purification, quantification, and characterization. The circulation of Anti-GBM antibody in glomerular basement membrane can be measured by the ELISA assay. In addition, the recombinant rat antigen is secreted in HEK293 cell supernatant which is purified by Anti-FLAG M2 monoclonal IgG antibody affinity column. In addition, it is characterized and quantified by SDS-PAGE gel electrophoresis and Western blotting techniques.

scholarly journals The prevalence and immunological features of anti-glomerular basement membrane antibody in patients with HIV

2020 ◽  
Author(s):  
Wenjing Wang ◽  
Xiao-yu Jia Jia ◽  
Zhao Cui ◽  
Yan Chen ◽  
Wei Wang ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Solid Phase ◽  
Chimeric Protein ◽  
Kidney Injury ◽  
Enzyme Linked Immunosorbent Assay ◽  
Hiv Viral Load ◽  
Hiv Patients ◽  
Type Iv

Abstract Background: Anti-glomerular basement membrane disease (GBM) is a kind of chronic autoimmune disease caused by the deposition of circulating anti-GBM antibodies. Non-collagen region of α3 chain of type IV collagen (α3(IV)NC1) is one of the main target antigens. And on α3, EA and EB are the most classical antigen epitopes. It has been reported that anti-GBM antibodies can be detected in HIV patients, but its immunological characteristics are still unclear. In this study, the immunological characteristics of the target antigens were clarified. Methods: Total 93 HIV patients and 20 healthy volunteers were selected in Beijing Youan Hospital from 2017 to 2018. Recombinant human α1-α5(IV)NC1, chimeric protein EA and EB were used as solid phase antigens. Enzyme-linked immunosorbent assay was employed to measure concentrations and subtypes of serum IgG autoantibodies specifically against GBM.Results: Five out of the 93 patients with HIV had low to moderate levels of anti-GBM antibodies. However, these patients presented with no clinical manifestation of any kidney injury or pulmonary hemorrhages. Compared with HIV patients with negative antibodies, there were no significant differences in gender, age, CD4+T cell count and HIV viral load. All sera of five patients recognized non-collagenous domain1 (NC1) of alpha 3 chain of type IV collagen [(α3(IV)NC1] as classic anti-GBM patients, followed by α5(IV)NC1. The antibodies against α3(IV)NC1 were IgG3 predominant, but did not react with either of the classic epitopes on α3 (EA and EB).Conclusion: These data suggest a distinct immunological profile of anti-GBM antibodies in patients with HIV, and might explain the non-pathogenic features of HIV associated anti-GBM antibodies.

A Case of IgA Nephropathy with Split Reduction of α5(V) Chain of Type IV Collagen in Glomerular Basement Membrane

Nephron ◽  
1998 ◽  
Vol 80 (4) ◽  
pp. 482-483 ◽  
Author(s):  
Shigeru Horita ◽  
Kosaku Nitta ◽  
Kazuho Honda ◽  
Hideo Kobayashi ◽  
Keiko Uchida ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Iga Nephropathy ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Type Iv

Platelet Interaction With Basement Membrane Proteins

1981 ◽  
Author(s):  
L Balleisen ◽  
J Rauterberg ◽  
J Risteli ◽  
H Rohde ◽  
R Timpl
Keyword(s):  
Membrane Proteins ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Fibrin Clot ◽  
Basement Membranes ◽  
Plastic Substrate ◽  
Acid Extraction ◽  
Clot Retraction ◽  
Type Iv ◽  
Basement Membrane Proteins

Basement membranes consist mainly of two components: non-fibrillar type IV collagen and the non-collagenous glycoprotein laminin (m.w.900.000) which is capable to interact with cell surfaces. The collagenous protein was studied in form of two major fragments comprising together the total mass of the molecule. 7-S collagen which resembles the crosslinking domain of type IV collagen was isolated after collagenase digestion and consisted of four triple helices aligned in a parallel fasion (m.w.360.000). The major triple helical domain of type IV collagen (m.w.450.000) could be obtained by a acid extraction but had lost most of the 7-S domain.Interaction with platelets was examined in aggregation, cell spreading and fibrin clot retraction assays including the determination of malondialdehyde formation. 7-S collagen was the most active component in all three assays. Aggregation was induced by as little as 25 µg/ml and was confirmed by electronmicroscopy. When compared to interstitial collagens, however, 10-20 fold higher amounts of 7-S collagen are required to produce the same effects. Acid extracted type IV collagen possessed virtually no activity. Laminin did not aggregate platelets but promoted strongly their attachment and spreading on a plastic substrate. Thus both basement membrane proteins apparently interact with platelets in different ways via distinct domains of the molecules.

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